ID   ADH1_CERCA              Reviewed;         257 AA.
AC   P48814;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
GN   Name=ADH1;
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Benakeion;
RX   PubMed=10732677; DOI=10.1007/pl00008679;
RA   Benos P., Tavernarakis N., Brogna S., Thireos G., Savakis C.;
RT   "Acquisition of a potential marker for insect transformation: isolation of
RT   a novel alcohol dehydrogenase gene from Bactrocera oleae by functional
RT   complementation in yeast.";
RL   Mol. Gen. Genet. 263:90-95(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; Z30194; CAA82926.1; -; Genomic_DNA.
DR   RefSeq; XP_004536079.1; XM_004536022.2.
DR   AlphaFoldDB; P48814; -.
DR   SMR; P48814; -.
DR   GeneID; 101454300; -.
DR   KEGG; ccat:101454300; -.
DR   OrthoDB; 1053465at2759; -.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   InterPro; IPR002426; ADH_Ceratitis-type.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR01169; CERATITISADH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..257
FT                   /note="Alcohol dehydrogenase 1"
FT                   /id="PRO_0000054448"
FT   ACT_SITE        150
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         9..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   257 AA;  27922 MW;  043F39AC1E09CACE CRC64;
     MSLAGKNVVF VGGLGFIAYE ACKYLMNNDL ASLFVFDVLD KPEAIKALQE INPKTKVYYT
     KFDITNKESI KQSLADVISK VQHIDALING AGILTDPNVE LTMNINLIGL INTTLEALPL
     MDKNKHGRGG VIVNIASVLG LEPCPPAAVY CASKFGVVGF SRSLGDPFYY EHTGVAVVTF
     CPGLTDTPLK NNIGSKYTFD YSKEIGEKLN SSKTQKPEVC GAHLAQAIEL MDNGAIYISN
     QGTLTKVKPS VYWEPTY